Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration-Reference-Cited by-同舟云学术

Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration

Published:2016 Issue:21 Volume:52 Page:4002-4005
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Xiang ShengQi¹²³⁴,Biernat Jacek⁵⁶⁷⁴⁸,Mandelkow Eckhard⁵⁶⁷⁴⁸,Becker Stefan¹²³⁴,Linser Rasmus¹²³⁴

Affiliation:

1. Max-Planck Institute for Biophysical Chemistry

2. Department NMR-Based Structural Biology

3. 37077 Göttingen

4. Germany

5. DZNE

6. German Center for Neurodegenerative Diseases

7. 53175 Bonn

8. CAESAR Research Center

Abstract

A set of higher-dimensionality ¹H-detected experiments is introduced for assigning non-deuterated proteins with low sample homogeneity at fast MAS.

Funder

Max-Planck-Gesellschaft

Verband der Chemischen Industrie

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CC/C5CC09160H

Reference37 articles.

1. High-Sensitivity Observation of Dipolar Exchange and NOEs between Exchangeable Protons in Proteins by 3D Solid-State NMR Spectroscopy

2. Ultrahigh Resolution in Proton Solid-State NMR Spectroscopy at High Levels of Deuteration

3. Fast Resonance Assignment and Fold Determination of Human Superoxide Dismutase by High-Resolution Proton-Detected Solid-State MAS NMR Spectroscopy

4. Solid-State NMR Structure Characterization of a 13CO-Labeled Ir(I) Complex with a P,N-Donor Ligand Including Ultrafast MAS Methods

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